[Interaction of acetyl-CoA carboxylase from the rat liver with analogs of activated carbon dioxide and ATP]. / Vzaimodeistvie atsetil-CoA-karboksilazy pecheni krys s analogami aktivirovannoi uglekisloty i ATP.
Mol Biol (Mosk)
; 22(1): 195-200, 1988.
Article
em Ru
| MEDLINE
| ID: mdl-2897623
ABSTRACT
The interaction of rat liver Ac-CoA-carboxylase with reactive and stable analogs of carbon dioxide and phosphoric acid mixed anhydrides--hypothetic intermediate of the enzyme reaction--has been studied. Carbamoylphosphate showed substrate properties, whereas phosphonacetic acid and beta-oxopropyl-alpha, alpha-diphosphonate inhibited this enzyme (Ki 3.0 and 3.5 mM correspondingly). The analog of another possible intermediate in the reaction of ATP and carbon dioxide, Appp (CH2COOH) also inhibited Ac-CoA-carboxylase (Ki = 0.7 mM).
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Base de dados:
MEDLINE
Assunto principal:
Acetato-CoA Ligase
/
Dióxido de Carbono
/
Trifosfato de Adenosina
/
Coenzima A Ligases
/
Fígado
Limite:
Animals
Idioma:
Ru
Revista:
Mol Biol (Mosk)
Ano de publicação:
1988
Tipo de documento:
Article